Our studies on the regulation of the lipid intermediate pathway of protein glycosylation in hormonally stimulated chick oviduct will continue along several lines. The ability of chick oviduct preparations (immature and hormone treated) to transfer oligosaccharide from exogenous (14C) oligosaccharide lipid to exogenous protein acceptors such as carboxymethylated goat alpha-lactalbumin will be assessed. Previous results obtained in our studies have indicated that preparation from immature chicks don't transfer (14C)Man or (14C)GlcNAc from sugar nucleotides to endogenous protein or oligosaccharide lipid. It is possible, however, that transfer doesn't occur because of the absence of oligosaccharide lipid synthesis, endogenous protein acceptors or the absence of the transferases. The experiments above should resolve these points. The biosynthesis of trisaccharide lipid (Man beta yields (GlcNAc)2PPDol) will also be studied as a function of hormone treatment. The trisaccharide lipid is the precursor for oligosaccharide lipid synthesis and the absence of oligosaccharide lipid biosynthesis in immature chick oviduct preparations may be the result of an absence of the mannosyltransferase. We will also study the biosynthesis of dolichol and dolichol phosphate from isopentenylpyrophosphate as well as dolichol and a kinase. Protein changes in the membrane during differentiation are being studied by double label SDS-gel electrophoresis.